Analysis of Weak Affinity of beta-D-Fructofuranosyl-(2 %26lt;-%26gt; 1)-2-acetamido-2-deoxy-alpha-D-glucopyranoside for Yeast beta-Fructofuranosidase Using NMR Spectroscopy

作者：Sakuma Chiseko; Furihata Kazuo; Nishio Toshiyuki; Miyakawa Takuya; Tanokura Masaru; Tashiro Mitsuru^*

来源：Journal of Carbohydrate Chemistry, 2014, 33(9): 498-505.

DOI：10.1080/07328303.2014.964407

• NMR
• Yeast beta-fructofuranosidase
• N-acetylsucrosamine
• Weak affinity

beta-D-Fructofuranosyl-(2 %26lt;-%26gt; 1)-2-acetamido-2-deoxy-alpha-D-glucopyranoside (N-acetylsucros-amine; SucNAc) is an enzymatic product from sucrose and 2-acetamido-2-deoxy-D-glucose (GlcNAc) and cannot be hydrolyzed by yeast beta-fructofuranosidase. Although the distinct binding of SucNAc with the beta-fructofuranosidase could not be identified by isothermal titration calorimetry or H-1 NMR titration, unambiguous signals indicating their molecular interactions were observed by STD NMR experiments. An inhibitory activity of SucNAc in the hydrolysis of sucrose was also confirmed by H-1 NMR spectroscopy. Because hydrolysis of sucrose was unaffected in the presence of GlcNAc, a disaccharide moiety including an acetamido group is considered to be crucial to show an inhibitory activity for the beta-fructofuranosidase.

• 出版日期2014-11-22